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Resumen Se investigaron los efectos del stress y la obesidad en diversos mecanismos fisiológicos hipotalámicos. La obesidad fué evidente inyectando aurothioglucose. Estadisticamente se registraron mayores aumentos en ratones aislados que en aquellos mantenidos familiarmente. 相似文献
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Modulation of A-type potassium channels by a family of calcium sensors 总被引:72,自引:0,他引:72
An WF Bowlby MR Betty M Cao J Ling HP Mendoza G Hinson JW Mattsson KI Strassle BW Trimmer JS Rhodes KJ 《Nature》2000,403(6769):553-556
In the brain and heart, rapidly inactivating (A-type) voltage-gated potassium (Kv) currents operate at subthreshold membrane potentials to control the excitability of neurons and cardiac myocytes. Although pore-forming alpha-subunits of the Kv4, or Shal-related, channel family form A-type currents in heterologous cells, these differ significantly from native A-type currents. Here we describe three Kv channel-interacting proteins (KChIPs) that bind to the cytoplasmic amino termini of Kv4 alpha-subunits. We find that expression of KChIP and Kv4 together reconstitutes several features of native A-type currents by modulating the density, inactivation kinetics and rate of recovery from inactivation of Kv4 channels in heterologous cells. All three KChIPs co-localize and co-immunoprecipitate with brain Kv4 alpha-subunits, and are thus integral components of native Kv4 channel complexes. The KChIPs have four EF-hand-like domains and bind calcium ions. As the activity and density of neuronal A-type currents tightly control responses to excitatory synaptic inputs, these KChIPs may regulate A-type currents, and hence neuronal excitability, in response to changes in intracellular calcium. 相似文献
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Frédéric?Delolme Cyril?Anastasi Lindsay?B.?Alcaraz Valentin?Mendoza Sandrine?Vadon-Le Goff Maya?Talantikite Robin?Capomaccio Jimmy?Mevaere La?titia?Fortin Dominique?Mazzocut Odile?Damour Isabelle?Zanella-Cléon David?J.?S.?Hulmes Christopher?M.?Overall Ulrich?Valcourt Fernando?Lopez-Casillas Catherine?MoaliEmail author 《Cellular and molecular life sciences : CMLS》2015,72(5):1009-1027
The metalloproteinase BMP-1 (bone morphogenetic protein-1) plays a major role in the control of extracellular matrix (ECM) assembly and growth factor activation. Most of the growth factors activated by BMP-1 are members of the TGF-β superfamily known to regulate multiple biological processes including embryonic development, wound healing, inflammation and tumor progression. In this study, we used an iTRAQ (isobaric tags for relative and absolute quantification)-based quantitative proteomic approach to reveal the release of proteolytic fragments from the cell surface or the ECM by BMP-1. Thirty-eight extracellular proteins were found in significantly higher or lower amounts in the conditioned medium of HT1080 cells overexpressing BMP-1 and thus, could be considered as candidate substrates. Strikingly, three of these new candidates (betaglycan, CD109 and neuropilin-1) were TGF-β co-receptors, also acting as antagonists when released from the cell surface, and were chosen for further substrate validation. Betaglycan and CD109 proved to be directly cleaved by BMP-1 and the corresponding cleavage sites were extensively characterized using a new mass spectrometry approach. Furthermore, we could show that the ability of betaglycan and CD109 to interact with TGF-β was altered after cleavage by BMP-1, leading to increased and prolonged SMAD2 phosphorylation in BMP-1-overexpressing cells. Betaglycan processing was also observed in primary corneal keratocytes, indicating a general and novel mechanism by which BMP-1 directly affects signaling by controlling TGF-β co-receptor activity. The proteomic data have been submitted to ProteomeXchange with the identifier PXD000786 and doi: 10.6019/PXD000786. 相似文献